Synthesis and functional properties of high-molecular-weight mannich bases

1977 ◽  
Vol 13 (9) ◽  
pp. 637-640
Author(s):  
V. P. Evstaf'ev ◽  
E. A. Ivanova ◽  
A. A. Fufaev ◽  
G. A. Trofimov ◽  
G. I. Shor ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Functional Properties ◽  
Mannich Bases

Influence of high-molecular-weight Mannich bases on the resorption of molybdenum from the gastrointestinal tract

1980 ◽  
Vol 14 (9) ◽  
pp. 617-620
Author(s):  
V. P. Borisov ◽  
V. M. Balakin ◽  
L. I. Seletskaya ◽  
V. V. Glukhikh
Keyword(s):  
Molecular Weight ◽  
Gastrointestinal Tract ◽  
High Molecular Weight ◽  
Mannich Bases

Transformation of wheat with high molecular weight subunit genes results in improved functional properties

1997 ◽  
Vol 15 (12) ◽  
pp. 1295-1299 ◽  
Author(s):  
Francisco Barro ◽  
Leonie Rooke ◽  
Frank Békés ◽  
Peter Gras ◽  
Arthur S. Tatham ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Functional Properties

Studies on Chemically Modified Fibrinogen

1976 ◽  
Vol 35 (02) ◽  
pp. 324-333 ◽  
Author(s):  
M Kloczewiak ◽  
Z Wegrzynowicz ◽  
F.R Matthias ◽  
D.L Heene ◽  
Maria Zajdel
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Functional Properties ◽  
Maleic Acid ◽  
Acid Anhydride ◽  
Polymerization Process ◽  
Chemically Modified ◽  
Fibrinogen Molecule

SummaryTreatment of fibrinogen with maleic acid anhydride renders fibrinogen unclottable depending on the degree of modification of the molecule. According to radioactive studies the release of fibrinopeptides by thrombin or reptilase is undisturbed. The incoagulability is due to inhibition of the polymerization process of fibrinmonomers derived from modified fibrinogen, mainly caused by the increase of electronegative charges upon the fibrinogen molecule. According to discelectrophoretic analysis modified fibrinogen fails to produce fragments D and E following plasmic digestion, however, may be degraded to high molecular weight products. Modified fibrinogen reveals some similarities to abnormal fibrinogens in congenital dysfibrinogenemia with regard to its functional properties.

scholarly journals Synthesis of New Blue Fluorescent Polymerizable 1,8-Naphthalimides and Their Copolymers with Styrene as Sensors for Fe(III) Cations

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Ivo Grabchev ◽  
Stanislava Yordanova ◽  
Stanimir Stoyanov ◽  
Ivan Petkov
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Functional Properties ◽  
Fluorescence Intensity ◽  
Metal Cations

The synthesis, characterization, and functional properties of two new polymerizable 1,8-naphthalimides (MDs) have been described. Their copolymers with styrene designed to act as a fluorescence PET chemosensor have been investigated. The study also reports the influence of different metal cations (Ag+, Mg2+, Cu2+, Sr2+, Co2+, Pb2+, and Fe3+) on the fluorescence intensity of both low and high molecular weight fluorophores.

Microtubule motors and other maps

1990 ◽  
Vol 48 (3) ◽  
pp. 1-1
Author(s):  
Richard B. Vallee
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytoplasmic Dynein ◽  
Organelle Transport ◽  
Structural Components ◽  
Microtubule Associated Proteins ◽  
Microtubule Motors ◽  
Associated Proteins ◽  
The Subject ◽  
Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

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